HMT1_SCHPO
ID HMT1_SCHPO Reviewed; 830 AA.
AC Q02592; O13675; Q9UQW7; Q9USI3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Heavy metal tolerance protein;
DE Flags: Precursor;
GN Name=hmt1; ORFNames=SPCC737.09c, SPCC74.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SP223;
RX PubMed=1396551; DOI=10.1002/j.1460-2075.1992.tb05431.x;
RA Ortiz D.F., Kreppel L., Speiser D.M., Scheel G., McDonald G., Ow D.W.;
RT "Heavy metal tolerance in the fission yeast requires an ATP-binding
RT cassette-type vacuolar membrane transporter.";
RL EMBO J. 11:3491-3499(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Involved in metal tolerance. Probably involved in the
CC transport of metal-bound phytochelatins. Compartmentalizes cadmium
CC within vacuoles, thereby protecting cells from cadmium toxicity.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
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DR EMBL; Z14055; CAA78419.1; -; mRNA.
DR EMBL; CU329672; CAA20865.1; -; Genomic_DNA.
DR PIR; S25198; S25198.
DR RefSeq; NP_588371.3; NM_001023362.3.
DR AlphaFoldDB; Q02592; -.
DR SMR; Q02592; -.
DR BioGRID; 280210; 22.
DR STRING; 4896.SPCC737.09c.1; -.
DR TCDB; 3.A.1.210.2; the atp-binding cassette (abc) superfamily.
DR MaxQB; Q02592; -.
DR PaxDb; Q02592; -.
DR PRIDE; Q02592; -.
DR EnsemblFungi; SPCC737.09c.1; SPCC737.09c.1:pep; SPCC737.09c.
DR GeneID; 3361134; -.
DR KEGG; spo:SPCC737.09c; -.
DR PomBase; SPCC737.09c; hmt1.
DR VEuPathDB; FungiDB:SPCC737.09c; -.
DR eggNOG; KOG0056; Eukaryota.
DR HOGENOM; CLU_000604_6_1_1; -.
DR InParanoid; Q02592; -.
DR OMA; WISVSQY; -.
DR PhylomeDB; Q02592; -.
DR Reactome; R-SPO-1369007; Mitochondrial ABC transporters.
DR Reactome; R-SPO-159418; Recycling of bile acids and salts.
DR Reactome; R-SPO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR Reactome; R-SPO-9754706; Atorvastatin ADME.
DR PRO; PR:Q02592; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0044604; F:ABC-type phytochelatin transporter activity; IMP:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0036249; P:cadmium ion import into vacuole; IMP:PomBase.
DR GO; GO:0098849; P:cellular detoxification of cadmium ion; IMP:PomBase.
DR GO; GO:0071996; P:glutathione transmembrane import into vacuole; IMP:PomBase.
DR GO; GO:0036246; P:phytochelatin 2 import into vacuole; IMP:PomBase.
DR GO; GO:0071995; P:phytochelatin import into vacuole; IMP:PomBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cadmium resistance; Glycoprotein; Membrane;
KW Nucleotide-binding; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT SIGNAL 1..27
FT CHAIN 28..830
FT /note="Heavy metal tolerance protein"
FT /id="PRO_0000000259"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 490..511
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 265..550
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 584..818
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 429..433
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 492..495
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 617..628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 79
FT /note="R -> A (in Ref. 1; CAA78419)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="S -> T (in Ref. 1; CAA78419)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="A -> R (in Ref. 1; CAA78419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 93994 MW; 909FBD10D51F50A9 CRC64;
MVLRYNSPRL NILELVLLYV GFFSIGSLNL LQKRKATSDP YRRKNRFGKE PIGIISWWIL
GIALTYVVDI SNLVIYALRV PNWWPCKTTV VCLILFLLFW IIVLISCADS KALPKNADSI
LKAYRLSVLY VWAIDIVFET IFIVYSPHPN ETFQGIVLAD HVARLVLCVF ATAIYLTYRR
KRHTHDPLDF EERQLTEESN VNENAISQNP STVQLGVSAS TSNFGTLKST SKKPSDKSWA
EYFRSFSTLL PYLWPTKDYR LQFQIFICIV LLFLGRAVNI LAPRQLGVLT EKLTKHSEKI
PWSDVILFVI YRFLQGNMGV IGSLRSFLWV PVSQYAYRAI STKALRHVLN LSYDFHLNKR
AGEVLTALTK GSSLNTFAEQ VVFQIGPVLL DLGVAMVYFF IKFDIYFTLI VLIMTLCYCY
VTVKITSWRT EARRKMVNSW RESYAVQNDA IMNFETVKNF DADDFENERY GHAVDIYLKQ
ERKVLFSLNF LNIVQGGIFT FSLAIACLLS AYRVTFGFNT VGDFVILLTY MIQLQQPLNF
FGTLYRSLQN SIIDTERLLE IFEEKPTVVE KPNAPDLKVT QGKVIFSHVS FAYDPRKPVL
SDINFVAQPG KVIALVGESG GGKSTIMRIL LRFFDVNSGS ITIDDQDIRN VTLSSLRSSI
GVVPQDSTLF NDTILYNIKY AKPSATNEEI YAAAKAAQIH DRILQFPDGY NSRVGERGLK
LSGGEKQRVA VARAILKDPS IILLDEATSA LDTNTERQIQ AALNRLASGR TAIVIAHRLS
TITNADLILC ISNGRIVETG THEELIKRDG GAYKKMWFQQ AMGKTSAETH
